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Journal of Biochemistry Advance Access published online on June 24, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp095
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© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Changes in the conformation of the Vsr endonuclease amino-terminal domain accompany DNA cleavage.

Yaroslava Y. Polosina and Claire G. Cupples

Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada

To whom correspondence should be addressed: Yaroslava Y. Polosina, University of Victoria, Department of Biochemistry and Microbiology, PO Box 3055 STN CSC, Victoria, BC, V8W 3P6, Canada Tel: (250) 721-8883, Fax: (250) 721-8855, E-mail: polosina{at}uvic.ca

Received March 16, 2009; Accepted June 15, 2009


  Abstract

In Escherichia coli, T/G mismatches arising from deamination of 5-methylcytosine to thymine are converted to CG base pairs by the very short patch repair pathway. DNA polymerase I removes and resynthesizes the mismatched T starting from a 5' nick created by the Vsr endonuclease. We used limited trypsinolysis to probe conformational changes in the N-terminal domain of Vsr in response to DNA binding, DNA cleavage and interaction with the polymerase. Our data show that the domain becomes trypsin resistant only under conditions that allow DNA cleavage, while interaction with the polymerase restores trypsin sensitivity. We suggest that the domain changes its conformation as a result of DNA nicking, and that DNA PolI releases Vsr from the nick by reversing that conformational change.

Key Words: Vsr endonuclease, VSP repair, DNA polymerase I, limited tryptic digestion


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